ID A0A366IPZ2_9MICO Unreviewed; 383 AA.
AC A0A366IPZ2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
GN ORFNames=DFO65_101139 {ECO:0000313|EMBL:RBP74421.1};
OS Brevibacterium celere.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=225845 {ECO:0000313|EMBL:RBP74421.1, ECO:0000313|Proteomes:UP000253509};
RN [1] {ECO:0000313|EMBL:RBP74421.1, ECO:0000313|Proteomes:UP000253509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3b_TX {ECO:0000313|EMBL:RBP74421.1,
RC ECO:0000313|Proteomes:UP000253509};
RA Lamendella R.;
RT "Freshwater and sediment microbial communities from various areas in North
RT America, analyzing microbe dynamics in response to fracking.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC glutamate--cysteine ligase activity. {ECO:0000256|HAMAP-Rule:MF_01609}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC Rule:MF_01609};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBP74421.1}.
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DR EMBL; QNSB01000001; RBP74421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366IPZ2; -.
DR Proteomes; UP000253509; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.590.20; -; 1.
DR HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011793; YbdK.
DR NCBIfam; TIGR02050; gshA_cyan_rel; 1.
DR PANTHER; PTHR36510; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR PANTHER; PTHR36510:SF1; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR Pfam; PF04107; GCS2; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01609, ECO:0000313|EMBL:RBP74421.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000253509}.
SQ SEQUENCE 383 AA; 42679 MW; 42CC7449BA8177C0 CRC64;
MVDFARSPRS TIGVEWELAL IDGHSLDLAP AAEDLLAAVA EHTPDFENRI VGEMLTNTIE
LVTGVHTDVP GIAADLSEAM ATLRTLTDPR GIELMCAGTH PFAQWQTQEI RPKDRYLELV
DRTQWWGRNM LIYGVHVHVG IDSRDKVLPI LNALLAYVPH LQALSASSPF WGGTDTGYAS
NRAMMFQQLP TAGLPFQFET WADYESYVED MLKTGIIDHI NEIRWDIRPS PHWGTVEVRV
CDGVPTLEEI SALTALIQCL VDDFSARLDA GETLPTMPDW FHAENKWRAA RYGMEAIIIE
NAAADERLVT ECLADEIERL GPTAERLGCL PELRSITALI ERGVSYQRQR EVFRTTGSLT
EVTRSLIGDL RSSKPCAVPA DRA
//